Nature Communications (Jun 2018)
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease
- Marthe H. R. Ludtmann,
- Plamena R. Angelova,
- Mathew H. Horrocks,
- Minee L. Choi,
- Margarida Rodrigues,
- Artyom Y. Baev,
- Alexey V. Berezhnov,
- Zhi Yao,
- Daniel Little,
- Blerida Banushi,
- Afnan Saleh Al-Menhali,
- Rohan T. Ranasinghe,
- Daniel R. Whiten,
- Ratsuda Yapom,
- Karamjit Singh Dolt,
- Michael J. Devine,
- Paul Gissen,
- Tilo Kunath,
- Morana Jaganjac,
- Evgeny V. Pavlov,
- David Klenerman,
- Andrey Y. Abramov,
- Sonia Gandhi
Affiliations
- Marthe H. R. Ludtmann
- Department of Molecular Neuroscience, UCL Institute of Neurology
- Plamena R. Angelova
- Department of Molecular Neuroscience, UCL Institute of Neurology
- Mathew H. Horrocks
- Department of Chemistry, University of Cambridge
- Minee L. Choi
- Sobell Department of Motor Neuroscience and Movement Disorders, UCL Institute of Neurology
- Margarida Rodrigues
- Department of Chemistry, University of Cambridge
- Artyom Y. Baev
- Educational-Experimental Centre of High Technologies, Laboratory of Biophysics and Biochemistry
- Alexey V. Berezhnov
- Institute of Cell Biophysics, Russian Academy of Sciences
- Zhi Yao
- Sobell Department of Motor Neuroscience and Movement Disorders, UCL Institute of Neurology
- Daniel Little
- MRC Laboratory for Molecular Cell Biology, University College London
- Blerida Banushi
- MRC Laboratory for Molecular Cell Biology, University College London
- Afnan Saleh Al-Menhali
- Toxicology and Multipurpose Department, Anti-Doping Lab Qatar, Sport City Road, PO Box 27775
- Rohan T. Ranasinghe
- Department of Chemistry, University of Cambridge
- Daniel R. Whiten
- Department of Chemistry, University of Cambridge
- Ratsuda Yapom
- MRC Centre for Regenerative Medicine, Institute for Stem Cell Research, School of Biological Sciences, The University of Edinburgh
- Karamjit Singh Dolt
- MRC Centre for Regenerative Medicine, Institute for Stem Cell Research, School of Biological Sciences, The University of Edinburgh
- Michael J. Devine
- MRC Laboratory for Molecular Cell Biology, University College London
- Paul Gissen
- MRC Laboratory for Molecular Cell Biology, University College London
- Tilo Kunath
- MRC Centre for Regenerative Medicine, Institute for Stem Cell Research, School of Biological Sciences, The University of Edinburgh
- Morana Jaganjac
- Toxicology and Multipurpose Department, Anti-Doping Lab Qatar, Sport City Road, PO Box 27775
- Evgeny V. Pavlov
- Department of Basic Sciences, New York University College of Dentistry
- David Klenerman
- Department of Chemistry, University of Cambridge
- Andrey Y. Abramov
- Department of Molecular Neuroscience, UCL Institute of Neurology
- Sonia Gandhi
- Sobell Department of Motor Neuroscience and Movement Disorders, UCL Institute of Neurology
- DOI
- https://doi.org/10.1038/s41467-018-04422-2
- Journal volume & issue
-
Vol. 9,
no. 1
pp. 1 – 16
Abstract
How toxic aggregated forms of α-synuclein lead to neurodegeneration is unclear. Here authors use biophysical and cellular imaging methods to show that specific oligomers of α-synuclein exert effects on mitochondria to induce opening of the permeability transition pore, leading to cell death in Parkinson’s disease.
